Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization

Occurrence of ϵ-poly- L-lysine-degrading enzyme in ϵ-poly- L-lysine-tolerant Sphingobacterium multivorum OJ10: purification and characterization

ϵ-Poly- L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released L-lysine. The enzyme was a Co...

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Veröffentlicht in:FEMS microbiology letters 2002-02, Vol.207 (2), p.147-151
Hauptverfasser: Kito, Mitsuaki, Onji, Yuichi, Yoshida, Toyokazu, Nagasawa, Toru
Format: Artikel
Sprache:eng
Schlagworte:
Aminopeptidase
Aminopeptidases - chemistry
Aminopeptidases - isolation & purification
Aminopeptidases - metabolism
Bacteriology
Biological and medical sciences
Flavobacterium - enzymology
Flavobacterium - isolation & purification
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Molecular Weight
Polylysine - metabolism
Sphingobacterium multivorum
Substrate Specificity
ϵ-Poly- L-lysine
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Zusammenfassung:ϵ-Poly- L-lysine (ϵ-PL)-degrading enzyme was found in the ϵ-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of ϵ-PL and released L-lysine. The enzyme was a Co 2+ or Ca 2+ ion-activated aminopeptidase.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(01)00571-7